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An in situ H₂O₂ generation approach to promote P450 peroxygenases catalysis was developed through the use of the nicotinamide cofactor analogue 1-benzyl-1,4-dihydronicotinamide (BNAH) and flavin mononucleotide (FMN). Final productivity could be enhanced due to higher enzyme stability at low H₂O₂ concentrations. The H₂O₂ generation represented the rate-limiting step, however it could be easily controlled by varying both FMN and BNAH concentrations. Further characterization can result in an optimized ratio of FMN/BNAH/O₂/biocatalyst enabling high reaction rates while minimizing H₂O₂-related inactivation of the enzyme.